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Article: Purification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4

TitlePurification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4
Authors
Issue Date2005
PublisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091
Citation
Acta Crystallographica Section F: Structural Biology And Crystallization Communications, 2005, v. 61 n. 3, p. 271-273 How to Cite?
AbstractDehIVa is one of two dehalogenases produced by the soil- and water-borne bacterium Burkholderia cepacia MBA4. It acts to break down short-chain halogenated aliphatic acids through a nucleophilic attack and subsequent hydrolysis of an enzyme-substrate intermediate to remove the halide ions from L-enantiomers substituted at the C2 position (e.g L-2-monochloropropionic acid). Dehalogenases are an important group of enzymes that are responsible for breaking down a diverse range of halogenated environmental pollutants. The dhlIVa gene coding for DehIVa was expressed in Escherichia coli and the protein was purified and crystallized using the hanging-drop method. Crystals grown in PEG 4000 and ammonium sulfate diffracted to 3.1 Å. crystals had a primitive hexagonal unit cell, with unit-cell parameters a = b = 104.2, c = 135.8 Å, α = β = 90, γ = 120°. Determining this structure will provide valuable insights into the characterization of the catalytic mechanisms of this group of enzymes. © 2005 International Union of Crystallography. All rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/48992
ISSN
2014 Impact Factor: 0.524
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorSchmidberger, JWen_HK
dc.contributor.authorOakley, AJen_HK
dc.contributor.authorTsang, JSHen_HK
dc.contributor.authorWilce, MCJen_HK
dc.date.accessioned2008-06-12T06:31:36Z-
dc.date.available2008-06-12T06:31:36Z-
dc.date.issued2005en_HK
dc.identifier.citationActa Crystallographica Section F: Structural Biology And Crystallization Communications, 2005, v. 61 n. 3, p. 271-273en_HK
dc.identifier.issn1744-3091en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48992-
dc.description.abstractDehIVa is one of two dehalogenases produced by the soil- and water-borne bacterium Burkholderia cepacia MBA4. It acts to break down short-chain halogenated aliphatic acids through a nucleophilic attack and subsequent hydrolysis of an enzyme-substrate intermediate to remove the halide ions from L-enantiomers substituted at the C2 position (e.g L-2-monochloropropionic acid). Dehalogenases are an important group of enzymes that are responsible for breaking down a diverse range of halogenated environmental pollutants. The dhlIVa gene coding for DehIVa was expressed in Escherichia coli and the protein was purified and crystallized using the hanging-drop method. Crystals grown in PEG 4000 and ammonium sulfate diffracted to 3.1 Å. crystals had a primitive hexagonal unit cell, with unit-cell parameters a = b = 104.2, c = 135.8 Å, α = β = 90, γ = 120°. Determining this structure will provide valuable insights into the characterization of the catalytic mechanisms of this group of enzymes. © 2005 International Union of Crystallography. All rights reserved.en_HK
dc.format.extent388 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherInternational Union of Crystallography. The Journal's web site is located at http://onlinelibrary.wiley.com/journal/10.1111/%28ISSN%291744-3091en_HK
dc.relation.ispartofActa Crystallographica Section F: Structural Biology and Crystallization Communicationsen_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.comen_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.subject.meshBacterial Proteins - chemistry - isolation & purificationen_HK
dc.subject.meshBurkholderia cepacia - enzymologyen_HK
dc.subject.meshHydrolases - chemistry - isolation & purificationen_HK
dc.subject.meshCrystallizationen_HK
dc.subject.meshRecombinant Proteins - chemistry - isolation & purificationen_HK
dc.titlePurification, crystallization and preliminary crystallographic analysis of DehIVa, a dehalogenase from Burkholderia cepacia MBA4en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1744-3091&volume=61&spage=271&epage=273&date=2005&atitle=Purification,+crystallization+and+preliminary+crystallographic+analysis+of+DehIVa,+a+dehalogenase+from+Burkholderia+cepacia+MBA4en_HK
dc.identifier.emailTsang, JSH: jshtsang@hku.hken_HK
dc.identifier.authorityTsang, JSH=rp00792en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.doi10.1107/S1744309105002472en_HK
dc.identifier.pmid16511015-
dc.identifier.pmcidPMC1952274en_HK
dc.identifier.scopuseid_2-s2.0-33646490138en_HK
dc.identifier.hkuros100600-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33646490138&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume61en_HK
dc.identifier.issue3en_HK
dc.identifier.spage271en_HK
dc.identifier.epage273en_HK
dc.identifier.isiWOS:000232293100005-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridSchmidberger, JW=13407197400en_HK
dc.identifier.scopusauthoridOakley, AJ=7005972539en_HK
dc.identifier.scopusauthoridTsang, JSH=7102483508en_HK
dc.identifier.scopusauthoridWilce, MCJ=7003621929en_HK
dc.identifier.citeulike90402-

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